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Control of collagen triple helix stability by phosphorylation

Control of collagen triple helix stability by phosphorylation
Control of collagen triple helix stability by phosphorylation
The phosphorylation of the collagen triple helix plays an important role in collagen synthesis, assembly, signaling, and immune response, although no reports detailing the effect this modification has on the structure and stability of the triple helix exist. Here we investigate the changes in stability and structure resulting from the phosphorylation of collagen. Additionally, the formation of pairwise interactions between phosphorylated residues and lysine is examined. In all tested cases, phosphorylation increases helix stability. When charged-pair interactions are possible, stabilization via phosphorylation can play a very large role, resulting inasmuch as a 13.0 °C increase in triple helix stability. Two-dimensional NMR and molecular modeling are used to study the local structure of the triple helix. Our results suggest a mechanism of action for phosphorylation in the regulation of collagen and also expand upon our understanding of pairwise amino acid stabilization of the collagen triple helix.
1525-7797
1157-1161
Acevedo-Jake, Amanda M.
648b12e3-763b-4e0b-bf33-abf4f85be1ef
Ngo, Daniel H.
52211611-a276-4608-befa-21aa949db7d4
Hartgerink, Jeffrey D.
37f5e1c8-1280-4133-8584-b327d6fcaaeb
Acevedo-Jake, Amanda M.
648b12e3-763b-4e0b-bf33-abf4f85be1ef
Ngo, Daniel H.
52211611-a276-4608-befa-21aa949db7d4
Hartgerink, Jeffrey D.
37f5e1c8-1280-4133-8584-b327d6fcaaeb

Acevedo-Jake, Amanda M., Ngo, Daniel H. and Hartgerink, Jeffrey D. (2017) Control of collagen triple helix stability by phosphorylation. Biomacromolecules, 18 (4), 1157-1161. (doi:10.1021/acs.biomac.6b01814).

Record type: Article

Abstract

The phosphorylation of the collagen triple helix plays an important role in collagen synthesis, assembly, signaling, and immune response, although no reports detailing the effect this modification has on the structure and stability of the triple helix exist. Here we investigate the changes in stability and structure resulting from the phosphorylation of collagen. Additionally, the formation of pairwise interactions between phosphorylated residues and lysine is examined. In all tested cases, phosphorylation increases helix stability. When charged-pair interactions are possible, stabilization via phosphorylation can play a very large role, resulting inasmuch as a 13.0 °C increase in triple helix stability. Two-dimensional NMR and molecular modeling are used to study the local structure of the triple helix. Our results suggest a mechanism of action for phosphorylation in the regulation of collagen and also expand upon our understanding of pairwise amino acid stabilization of the collagen triple helix.

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More information

e-pub ahead of print date: 10 March 2017
Published date: 10 April 2017

Identifiers

Local EPrints ID: 434653
URI: http://eprints.soton.ac.uk/id/eprint/434653
ISSN: 1525-7797
PURE UUID: da5c4282-4c11-4658-bf53-57fc73738633

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Date deposited: 04 Oct 2019 16:30
Last modified: 04 Oct 2019 16:30

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